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Titolo:
SUBSTITUTION OF AN AMINO-ACID RESIDUE BY ASP FOR CONFORMATIONAL CONSTRAINT OF LYS-XAA FRAGMENT IN BIOLOGICALLY-ACTIVE PEPTIDES BY SIDE-CHAIN LACTAMIZATION
Autore:
KOSTETSKY PV; ARTEMJEV IV;
Indirizzi:
RUSSIAN ACAD SCI,SHEMYAKIN OVCHINNIKOV INST BIOORGAN CHEM,UL MIKLUKHOMAKLAYA 16-10 MOSCOW 117871 RUSSIA
Titolo Testata:
Biochemistry
fascicolo: 7, volume: 62, anno: 1997,
pagine: 753 - 759
SICI:
0006-2979(1997)62:7<753:SOAARB>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
HORMONE RELEASING-FACTOR; CYCLIC LACTAM ANALOGS; MOLECULAR-DYNAMICS; CENTRAL RECEPTORS; SIMULATIONS; DESIGN; TETRAPEPTIDES; CYCLIZATION; PROTEINS; POTENT;
Keywords:
CYCLIC PEPTIDE; THEORETICAL CONFORMATIONAL ANALYSIS; THYMOPENTIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
P.V. Kostetsky e I.V. Artemjev, "SUBSTITUTION OF AN AMINO-ACID RESIDUE BY ASP FOR CONFORMATIONAL CONSTRAINT OF LYS-XAA FRAGMENT IN BIOLOGICALLY-ACTIVE PEPTIDES BY SIDE-CHAIN LACTAMIZATION", Biochemistry, 62(7), 1997, pp. 753-759

Abstract

The model cyclic peptide Ac-Lys-Asp-NHMe was used to test Asp as a possible substitute for Xaa in a peptide fragment Lys-Xaa whose conformational mobility would be constrained by lactamization of the Lys and Asp side chains. By means of theoretical conformational analysis, such a lactam was shown to be capable of fixing several conformations of a peptide. Among them, 32 conformations correspond to 8 low-energy regions of the linear peptide Ac-Ala-Ala-NHMe; this was chosen as a model for the peptide fragment Lys-Xaa. In this case, the conformational possibilities of the Lys residue were constrained to two regions of the phi,psi-map (A + G) and (C + F) according to Zimmerman-Scheraga notation. Dihedral angles phi and psi of the Asp residue correspond to lowest-energy areas of phi,psi-map for the Ala residue in linear peptides.

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Documento generato il 03/07/20 alle ore 16:08:26